Analytical Data
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Gene name
DSU
- Application
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Alternative Names
MREG. DSU. HDCGA21P
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N565
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Expression Region
1-214aa
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AA Sequence
MGLRDWLRTVCCCCGCECLEERALPEKEPLVSDNNPYSSFGATLVRDDEKNLWSMPHDVSHTEADDDRTLYNLIVIRNQQAKDSEEWQKLNYDIHTLRQVRREVRNRWKCILEDLGFQKEADSLLSVTKLSTISDSKNTRKAREMLLKLAEETNIFPTSWELSERYLFVVDRLIALDAAEEFFKLARRTYPKKPGVPCLADGQKELHYLPFPSP
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Molecular Weight
49.28 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The protein DSU (Dihydrofolate Synthase-Urease) is a recombinant enzyme that has garnered significant attention in the field of molecular biology and biotechnology due to its dual functionalities in catalyzing specific biochemical reactions. The study of DSU is driven by its potential applications in various industrial processes, including pharmaceuticals and agriculture. Researchers are particularly interested in its role in folate metabolism and nitrogen fixation. Given the global challenges posed by nutrient deficiency and environmental sustainability, the ability to engineer and optimize such enzymes could pave the way for innovative solutions to enhance crop yield and reduce chemical fertilizer dependency. Furthermore, recombinant technology allows for the modification of DSU to improve its stability and activity under diverse conditions. This research not only contributes to the fundamental understanding of enzyme mechanisms but also opens avenues for biotechnological advancements. Consequently, extensive investigations into the structure, function, and optimization of DSU continue to be crucial as they hold promise for practical applications in promoting sustainable agriculture and addressing pressing food security issues worldwide.
